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Database: PDB
Entry: 1CO7
LinkDB: 1CO7
Original site: 1CO7 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           07-JUN-99   1CO7              
TITLE     R117H MUTANT RAT ANIONIC TRYPSIN COMPLEXED WITH BOVINE                
TITLE    2 PANCREATIC TRYPSIN INHIBITOR (BPTI)                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN II;                                                
COMPND   3 CHAIN: E;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BOVINE PANCREATIC TRYPSIN INHIBITOR;                       
COMPND   8 CHAIN: I;                                                            
COMPND   9 SYNONYM: BPTI                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   7 ORGANISM_COMMON: CATTLE;                                             
SOURCE   8 ORGANISM_TAXID: 9913                                                 
KEYWDS    COMPLEX (SERINE PROTEASE/INHIBITOR), HYDROLASE/HYDROLASE              
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.F.STAMPER,D.RINGE,L.HEDSTROM                                        
REVDAT   3   24-FEB-09 1CO7    1       VERSN                                    
REVDAT   2   28-FEB-06 1CO7    1       JRNL   REMARK                            
REVDAT   1   07-JAN-03 1CO7    0                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21149                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2105                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2182                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 247                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.005                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1995                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 103                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.58                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CA.PAR                                         
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : CA.TOP                                         
REMARK   3  TOPOLOGY FILE  3   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CO7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB001155.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200HB                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22249                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.37900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: 3TGI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.60400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.80200            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       20.80200            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.60400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 WARNING: SEQUENTIALLY DISTANT RESIDUE (I ASN 24 )                    
REMARK 400 AND RESIDUE (I LEU 29 ) ARE LINKED TOGETHER,                         
REMARK 400 DISTANCE ASN24I.C-LEU29I.N: 1.319A                                   
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG E    -6                                                      
REMARK 465     ALA E    -5                                                      
REMARK 465     LEU E    -4                                                      
REMARK 465     LEU E    -3                                                      
REMARK 465     PHE E    -2                                                      
REMARK 465     LEU E    -1                                                      
REMARK 465     ALA E     0                                                      
REMARK 465     LEU E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     ALA E     4                                                      
REMARK 465     ALA E     5                                                      
REMARK 465     VAL E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     PHE E     8                                                      
REMARK 465     PRO E     9                                                      
REMARK 465     VAL E    10                                                      
REMARK 465     ASP E    11                                                      
REMARK 465     ASP E    12                                                      
REMARK 465     ASP E    13                                                      
REMARK 465     ASP E    14                                                      
REMARK 465     LYS E    15                                                      
REMARK 465     LYS I   -33                                                      
REMARK 465     MET I   -32                                                      
REMARK 465     SER I   -31                                                      
REMARK 465     ARG I   -30                                                      
REMARK 465     LEU I   -29                                                      
REMARK 465     CYS I   -28                                                      
REMARK 465     LEU I   -27                                                      
REMARK 465     SER I   -26                                                      
REMARK 465     VAL I   -25                                                      
REMARK 465     ALA I   -24                                                      
REMARK 465     LEU I   -23                                                      
REMARK 465     LEU I   -22                                                      
REMARK 465     VAL I   -21                                                      
REMARK 465     LEU I   -20                                                      
REMARK 465     LEU I   -19                                                      
REMARK 465     GLY I   -18                                                      
REMARK 465     THR I   -17                                                      
REMARK 465     LEU I   -16                                                      
REMARK 465     ALA I   -15                                                      
REMARK 465     ALA I   -14                                                      
REMARK 465     SER I   -13                                                      
REMARK 465     THR I   -12                                                      
REMARK 465     PRO I   -11                                                      
REMARK 465     GLY I   -10                                                      
REMARK 465     CYS I    -9                                                      
REMARK 465     ASP I    -8                                                      
REMARK 465     THR I    -7                                                      
REMARK 465     SER I    -6                                                      
REMARK 465     ASN I    -5                                                      
REMARK 465     GLN I    -4                                                      
REMARK 465     ALA I    -3                                                      
REMARK 465     LYS I    -2                                                      
REMARK 465     ALA I    -1                                                      
REMARK 465     GLN I     0                                                      
REMARK 465     ARG I     1                                                      
REMARK 465     PRO I     2                                                      
REMARK 465     ASP I     3                                                      
REMARK 465     PHE I     4                                                      
REMARK 465     CYS I     5                                                      
REMARK 465     LEU I     6                                                      
REMARK 465     GLU I     7                                                      
REMARK 465     PRO I     8                                                      
REMARK 465     ALA I    25                                                      
REMARK 465     LYS I    26                                                      
REMARK 465     ALA I    27                                                      
REMARK 465     GLY I    28                                                      
REMARK 465     THR I    54                                                      
REMARK 465     CYS I    55                                                      
REMARK 465     GLY I    56                                                      
REMARK 465     GLY I    57                                                      
REMARK 465     ALA I    58                                                      
REMARK 465     ILE I    59                                                      
REMARK 465     GLY I    60                                                      
REMARK 465     PRO I    61                                                      
REMARK 465     TRP I    62                                                      
REMARK 465     GLU I    63                                                      
REMARK 465     ASN I    64                                                      
REMARK 465     LEU I    65                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG I  42    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN E    25     ND1  HIS E   117              2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASN I  24   N   -  CA  -  C   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    LEU I  29   N   -  CA  -  C   ANGL. DEV. = -32.8 DEGREES          
REMARK 500    ARG I  53   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG I  53   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN E  25       47.85     30.01                                   
REMARK 500    ASP E  49       -4.65    -55.51                                   
REMARK 500    HIS E  71      -58.77   -134.91                                   
REMARK 500    SER E 214      -66.92   -122.46                                   
REMARK 500    ASN I  24      -50.81   -142.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 800  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  70   OE1                                                    
REMARK 620 2 ASN E  72   O    93.4                                              
REMARK 620 3 VAL E  75   O   154.2  84.7                                        
REMARK 620 4 GLU E  77   OE1 102.1  95.4 103.6                                  
REMARK 620 5 GLU E  80   OE2 100.8 165.8  83.1  80.5                            
REMARK 620 6 HOH E 438   O    75.7 112.0  81.3 152.6  73.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: THE CATALYTIC TRIAD                                
REMARK 800 SITE_IDENTIFIER: P1                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: THE INHIBITOR RESIDUE IN THE PRIMARY               
REMARK 800  SPECIFICITY SITE                                                    
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 800                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 1CO7 E SWS P00763  -6 - 15 NOT IN ATOMS LIST                         
REMARK 999 1CO7 I SWS P00974 -33 -  8 NOT IN ATOMS LIST                         
REMARK 999 1CO7 I SWS P00974  25 - 28 NOT IN ATOMS LIST                         
REMARK 999 1CO7 I SWS P00974  54 - 65 NOT IN ATOMS LIST                         
REMARK 999                                                                      
REMARK 999 WHILE SWISS-PROT NUMBERING IS CONSECUTIVE, PDB                       
REMARK 999 SEGMENT IS NUMBERED TO PROVIDE MAXIMUM HOMOLOGY                      
REMARK 999 WITH CHYMOTRYPSIN.                                                   
DBREF  1CO7 E   -6   245  UNP    P00763   TRY2_RAT         2    246             
DBREF  1CO7 I  -33    65  UNP    P00974   BPT1_BOVIN       2    100             
SEQADV 1CO7 HIS E  117  UNP  P00763    ARG   121 VARIANT                        
SEQRES   1 E  245  ARG ALA LEU LEU PHE LEU ALA LEU VAL GLY ALA ALA VAL          
SEQRES   2 E  245  ALA PHE PRO VAL ASP ASP ASP ASP LYS ILE VAL GLY GLY          
SEQRES   3 E  245  TYR THR CYS GLN GLU ASN SER VAL PRO TYR GLN VAL SER          
SEQRES   4 E  245  LEU ASN SER GLY TYR HIS PHE CYS GLY GLY SER LEU ILE          
SEQRES   5 E  245  ASN ASP GLN TRP VAL VAL SER ALA ALA HIS CYS TYR LYS          
SEQRES   6 E  245  SER ARG ILE GLN VAL ARG LEU GLY GLU HIS ASN ILE ASN          
SEQRES   7 E  245  VAL LEU GLU GLY ASN GLU GLN PHE VAL ASN ALA ALA LYS          
SEQRES   8 E  245  ILE ILE LYS HIS PRO ASN PHE ASP ARG LYS THR LEU ASN          
SEQRES   9 E  245  ASN ASP ILE MET LEU ILE LYS LEU SER SER PRO VAL LYS          
SEQRES  10 E  245  LEU ASN ALA HIS VAL ALA THR VAL ALA LEU PRO SER SER          
SEQRES  11 E  245  CYS ALA PRO ALA GLY THR GLN CYS LEU ILE SER GLY TRP          
SEQRES  12 E  245  GLY ASN THR LEU SER SER GLY VAL ASN GLU PRO ASP LEU          
SEQRES  13 E  245  LEU GLN CYS LEU ASP ALA PRO LEU LEU PRO GLN ALA ASP          
SEQRES  14 E  245  CYS GLU ALA SER TYR PRO GLY LYS ILE THR ASP ASN MET          
SEQRES  15 E  245  VAL CYS VAL GLY PHE LEU GLU GLY GLY LYS ASP SER CYS          
SEQRES  16 E  245  GLN GLY ASP SER GLY GLY PRO VAL VAL CYS ASN GLY GLU          
SEQRES  17 E  245  LEU GLN GLY ILE VAL SER TRP GLY TYR GLY CYS ALA LEU          
SEQRES  18 E  245  PRO ASP ASN PRO GLY VAL TYR THR LYS VAL CYS ASN TYR          
SEQRES  19 E  245  VAL ASP TRP ILE GLN ASP THR ILE ALA ALA ASN                  
SEQRES   1 I   99  LYS MET SER ARG LEU CYS LEU SER VAL ALA LEU LEU VAL          
SEQRES   2 I   99  LEU LEU GLY THR LEU ALA ALA SER THR PRO GLY CYS ASP          
SEQRES   3 I   99  THR SER ASN GLN ALA LYS ALA GLN ARG PRO ASP PHE CYS          
SEQRES   4 I   99  LEU GLU PRO PRO TYR THR GLY PRO CYS LYS ALA ARG ILE          
SEQRES   5 I   99  ILE ARG TYR PHE TYR ASN ALA LYS ALA GLY LEU CYS GLN          
SEQRES   6 I   99  THR PHE VAL TYR GLY GLY CYS ARG ALA LYS ARG ASN ASN          
SEQRES   7 I   99  PHE LYS SER ALA GLU ASP CYS MET ARG THR CYS GLY GLY          
SEQRES   8 I   99  ALA ILE GLY PRO TRP GLU ASN LEU                              
HET     CA  E 800       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *103(H2 O)                                                    
HELIX    1   1 ALA E   56  CYS E   58  5                                   3    
HELIX    2   2 GLN E  165  SER E  171  1                                   7    
HELIX    3   3 VAL E  231  ASN E  233  5                                   3    
HELIX    4   4 VAL E  235  ALA E  243  1                                   9    
HELIX    5   5 ALA I   48  CYS I   51  1                                   4    
SHEET    1   A 7 GLN E  81  ASN E  84  0                                        
SHEET    2   A 7 GLN E  64  LEU E  68 -1  N  LEU E  68   O  GLN E  81           
SHEET    3   A 7 GLN E  30  ASN E  34 -1  N  ASN E  34   O  GLN E  64           
SHEET    4   A 7 HIS E  40  ASN E  48 -1  N  GLY E  44   O  VAL E  31           
SHEET    5   A 7 TRP E  51  SER E  54 -1  N  VAL E  53   O  SER E  45           
SHEET    6   A 7 MET E 104  LEU E 108 -1  N  ILE E 106   O  VAL E  52           
SHEET    7   A 7 ALA E  85  LYS E  90 -1  N  ILE E  89   O  LEU E 105           
SHEET    1   B 2 GLN E 135  GLY E 140  0                                        
SHEET    2   B 2 GLN E 156  PRO E 161 -1  N  ALA E 160   O  CYS E 136           
SHEET    1   C 4 MET E 180  VAL E 183  0                                        
SHEET    2   C 4 GLY E 226  LYS E 230 -1  N  TYR E 228   O  VAL E 181           
SHEET    3   C 4 GLU E 204  TRP E 215 -1  N  TRP E 215   O  VAL E 227           
SHEET    4   C 4 PRO E 198  CYS E 201 -1  N  CYS E 201   O  GLU E 204           
SHEET    1   D 2 ILE I  18  PHE I  22  0                                        
SHEET    2   D 2 GLN I  31  TYR I  35 -1  N  TYR I  35   O  ILE I  18           
SSBOND   1 CYS E   22    CYS E  157                          1555   1555  2.04  
SSBOND   2 CYS E   42    CYS E   58                          1555   1555  2.03  
SSBOND   3 CYS E  128    CYS E  232                          1555   1555  2.03  
SSBOND   4 CYS E  136    CYS E  201                          1555   1555  2.02  
SSBOND   5 CYS E  168    CYS E  182                          1555   1555  2.02  
SSBOND   6 CYS E  191    CYS E  220                          1555   1555  2.03  
SSBOND   7 CYS I   14    CYS I   38                          1555   1555  2.04  
SSBOND   8 CYS I   30    CYS I   51                          1555   1555  2.03  
LINK         OE1 GLU E  70                CA    CA E 800     1555   1555  2.44  
LINK         O   ASN E  72                CA    CA E 800     1555   1555  2.34  
LINK         O   VAL E  75                CA    CA E 800     1555   1555  2.29  
LINK         OE1 GLU E  77                CA    CA E 800     1555   1555  2.60  
LINK         OE2 GLU E  80                CA    CA E 800     1555   1555  2.46  
LINK        CA    CA E 800                 O   HOH E 438     1555   1555  3.03  
SITE     1 CAT  3 HIS E  57  ASP E 102  SER E 195                               
SITE     1  P1  1 LYS I  15                                                     
SITE     1 AC1  6 GLU E  70  ASN E  72  VAL E  75  GLU E  77                    
SITE     2 AC1  6 GLU E  80  HOH E 438                                          
CRYST1   92.696   92.696   62.406  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010788  0.006228  0.000000        0.00000                         
SCALE2      0.000000  0.012457  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016024        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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